GRAS_STAA9
ID GRAS_STAA9 Reviewed; 346 AA.
AC A5IQL3;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Sensor protein kinase GraS;
DE EC=2.7.13.3;
DE AltName: Full=Glycopeptide resistance-associated protein S;
GN Name=graS; OrderedLocusNames=SaurJH9_0683;
OS Staphylococcus aureus (strain JH9).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=359786;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JH9;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Tomasz A., Richardson P.;
RT "Complete sequence of chromosome of Staphylococcus aureus subsp. aureus
RT JH9.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Member of the two-component regulatory system GraR/GraS
CC involved in resistance against cationic antimicrobial peptides (CAMPs).
CC Functions as a sensor protein kinase which phosphorylates GraR through
CC the auxiliary protein GraX. In turn, GraR up-regulates many genes such
CC as adhesins, exoproteins, transporters, toxins, and proteins involved
CC in cell wall synthesis. Down-regulates the expression of many genes
CC involved in RNA and amino acid synthesis or glycolysis.
CC {ECO:0000250|UniProtKB:Q2G0D9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBUNIT: Interacts with GraX. {ECO:0000250|UniProtKB:Q2G0D9}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; CP000703; ABQ48486.1; -; Genomic_DNA.
DR RefSeq; WP_001061264.1; NC_009487.1.
DR AlphaFoldDB; A5IQL3; -.
DR SMR; A5IQL3; -.
DR KEGG; saj:SaurJH9_0683; -.
DR HOGENOM; CLU_000445_13_1_9; -.
DR OMA; YEWLRIH; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; ATP-binding; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system; Virulence.
FT CHAIN 1..346
FT /note="Sensor protein kinase GraS"
FT /id="PRO_0000347916"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 126..332
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 346 AA; 41032 MW; 42952E007DD7CDA8 CRC64;
MNNLKWVAYF LKSRMNWIFW ILFLNLLMLG ISLIDYDFPI DSLFYIVSLN LSLTMIFLIL
TYFKEVKLYK HFDKDKEIEE IKHKDLAETP FQRHTVDYLY RQISAHKEKV VEQQLQLNMH
EQTITEFVHD IKTPVTAMKL LIDQEKNQER KQALLYEWSR INSMLDTQLY ITRLESQRKD
MYFDYVSLKR MVIDEIQLTR HISQVKGIGF DVDFKVDDYV YTDTKWCRMI IRQILSNALK
YSENFNIEIG TELNDQHVSL YIKDYGRGIS KKDMPRIFER GFTSTANRNE TTSSGMGLYL
VNSVKDQLGI HLQVTSTVGK GTTVRLIFPL QNEIVERMSE VTNLSF